spacer
spacer

PDBsum entry 3eyx

Go to PDB code: 
Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
3eyx
Jmol
Contents
Protein chains
197 a.a.
Ligands
ACT ×2
EDO ×4
Metals
_ZN ×2
Waters ×152
HEADER    LYASE                                   22-OCT-08   3EYX
TITLE     CRYSTAL STRUCTURE OF CARBONIC ANHYDRASE NCE103 FROM
TITLE    2 SACCHAROMYCES CEREVISIAE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: RESIDUES 14-221;
COMPND   5 SYNONYM: BETA-CARBONIC ANHYDRASE, CARBONATE DEHYDRATASE,
COMPND   6 NON-CLASSICAL EXPORT PROTEIN 3;
COMPND   7 EC: 4.2.1.1;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE   4 ORGANISM_TAXID: 4932;
SOURCE   5 STRAIN: S288C;
SOURCE   6 GENE: NCE103;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: ROSETTA DE3;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: P29
KEYWDS    ROSSMANN FOLD, CYTOPLASM, LYASE, METAL-BINDING, NUCLEUS,
KEYWDS   2 ZINC
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.B.TENG,Y.L.JIANG,Y.CHEN,C.Z.ZHOU
REVDAT   2   02-FEB-10 3EYX    1       JRNL
REVDAT   1   15-SEP-09 3EYX    0
JRNL        AUTH   Y.B.TENG,Y.L.JIANG,Y.X.HE,W.W.HE,F.M.LIAN,Y.CHEN,
JRNL        AUTH 2 C.Z.ZHOU
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE SUBSTRATE TUNNEL OF
JRNL        TITL 2 SACCHAROMYCES CEREVISIAE CARBONIC ANHYDRASE NCE103.
JRNL        REF    BMC STRUCT.BIOL.              V.   9    67 2009
JRNL        REFN                   ESSN 1472-6807
JRNL        PMID   19852838
JRNL        DOI    10.1186/1472-6807-9-67
REMARK   2
REMARK   2 RESOLUTION.    2.04 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.04
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 16.11
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.2
REMARK   3   NUMBER OF REFLECTIONS             : 24369
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.199
REMARK   3   R VALUE            (WORKING SET) : 0.197
REMARK   3   FREE R VALUE                     : 0.241
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1288
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.04
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1630
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.15
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2190
REMARK   3   BIN FREE R VALUE SET COUNT          : 89
REMARK   3   BIN FREE R VALUE                    : 0.2760
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3130
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 26
REMARK   3   SOLVENT ATOMS            : 152
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.72
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.85000
REMARK   3    B22 (A**2) : 0.90000
REMARK   3    B33 (A**2) : -0.05000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.228
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.189
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.118
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.185
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.938
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.908
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3208 ; 0.010 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4340 ; 1.107 ; 1.949
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   390 ; 5.004 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   150 ;38.755 ;25.600
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   566 ;12.668 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;15.433 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   504 ; 0.078 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2376 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1579 ; 0.189 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2214 ; 0.292 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   204 ; 0.116 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.031 ; 0.200
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    75 ; 0.185 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.166 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2044 ; 0.778 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3192 ; 0.923 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1330 ; 1.575 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1148 ; 2.226 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3EYX COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-OCT-08.
REMARK 100 THE RCSB ID CODE IS RCSB049941.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-07
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25657
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.030
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.1
REMARK 200  DATA REDUNDANCY                : 2.800
REMARK 200  R MERGE                    (I) : 0.06600
REMARK 200  R SYM                      (I) : 0.08100
REMARK 200   FOR THE DATA SET  : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.31000
REMARK 200  R SYM FOR SHELL            (I) : 0.38300
REMARK 200   FOR SHELL         : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1DDZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 0.2M SODIUM ACETATE,
REMARK 280  0.1M SODIUM CITRATE, 20% ETHYLENE GLYCOL , PH 5.6, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       44.84500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       44.84500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       30.28500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       77.86500
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       30.28500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       77.86500
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       44.84500
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       30.28500
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       77.86500
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       44.84500
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       30.28500
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       77.86500
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -111.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     6
REMARK 465     HIS A     7
REMARK 465     HIS A     8
REMARK 465     HIS A     9
REMARK 465     HIS A    10
REMARK 465     HIS A    11
REMARK 465     HIS A    12
REMARK 465     GLY A    13
REMARK 465     HIS A    14
REMARK 465     ASN A    15
REMARK 465     SER A    16
REMARK 465     PRO A    41
REMARK 465     ASP A    42
REMARK 465     HIS A    43
REMARK 465     ASN A    44
REMARK 465     ALA A    45
REMARK 465     LYS A    46
REMARK 465     GLY A    47
REMARK 465     GLN A    48
REMARK 465     MET B     6
REMARK 465     HIS B     7
REMARK 465     HIS B     8
REMARK 465     HIS B     9
REMARK 465     HIS B    10
REMARK 465     HIS B    11
REMARK 465     HIS B    12
REMARK 465     GLY B    13
REMARK 465     HIS B    14
REMARK 465     ASN B    15
REMARK 465     SER B    16
REMARK 465     PRO B    41
REMARK 465     ASP B    42
REMARK 465     HIS B    43
REMARK 465     ASN B    44
REMARK 465     ALA B    45
REMARK 465     LYS B    46
REMARK 465     GLY B    47
REMARK 465     GLN B    48
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASP A  59      129.32    -32.94
REMARK 500    ASN A  82       50.39     35.82
REMARK 500    ASP B  59      129.08    -35.90
REMARK 500    ASN B  63     -161.32   -161.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A   1  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A  57   SG
REMARK 620 2 HIS A 112   NE2 111.5
REMARK 620 3 CYS A 115   SG  121.2 108.9
REMARK 620 4 HOH A 263   O   105.8  93.9 112.1
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B   2  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B  57   SG
REMARK 620 2 HIS B 112   NE2 112.8
REMARK 620 3 CYS B 115   SG  122.5 108.5
REMARK 620 4 HOH A 300   O   108.0  91.3 109.3
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 222
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 222
DBREF  3EYX A   14   221  UNP    P53615   CAN_YEAST       14    221
DBREF  3EYX B   14   221  UNP    P53615   CAN_YEAST       14    221
SEQADV 3EYX MET A    6  UNP  P53615              INITIATING METHIONINE
SEQADV 3EYX HIS A    7  UNP  P53615              EXPRESSION TAG
SEQADV 3EYX HIS A    8  UNP  P53615              EXPRESSION TAG
SEQADV 3EYX HIS A    9  UNP  P53615              EXPRESSION TAG
SEQADV 3EYX HIS A   10  UNP  P53615              EXPRESSION TAG
SEQADV 3EYX HIS A   11  UNP  P53615              EXPRESSION TAG
SEQADV 3EYX HIS A   12  UNP  P53615              EXPRESSION TAG
SEQADV 3EYX GLY A   13  UNP  P53615              EXPRESSION TAG
SEQADV 3EYX MET B    6  UNP  P53615              INITIATING METHIONINE
SEQADV 3EYX HIS B    7  UNP  P53615              EXPRESSION TAG
SEQADV 3EYX HIS B    8  UNP  P53615              EXPRESSION TAG
SEQADV 3EYX HIS B    9  UNP  P53615              EXPRESSION TAG
SEQADV 3EYX HIS B   10  UNP  P53615              EXPRESSION TAG
SEQADV 3EYX HIS B   11  UNP  P53615              EXPRESSION TAG
SEQADV 3EYX HIS B   12  UNP  P53615              EXPRESSION TAG
SEQADV 3EYX GLY B   13  UNP  P53615              EXPRESSION TAG
SEQRES   1 A  216  MET HIS HIS HIS HIS HIS HIS GLY HIS ASN SER ASN LEU
SEQRES   2 A  216  GLN ASP ILE LEU ALA ALA ASN ALA LYS TRP ALA SER GLN
SEQRES   3 A  216  MET ASN ASN ILE GLN PRO THR LEU PHE PRO ASP HIS ASN
SEQRES   4 A  216  ALA LYS GLY GLN SER PRO HIS THR LEU PHE ILE GLY CYS
SEQRES   5 A  216  SER ASP SER ARG TYR ASN GLU ASN CYS LEU GLY VAL LEU
SEQRES   6 A  216  PRO GLY GLU VAL PHE THR TRP LYS ASN VAL ALA ASN ILE
SEQRES   7 A  216  CYS HIS SER GLU ASP LEU THR LEU LYS ALA THR LEU GLU
SEQRES   8 A  216  PHE ALA ILE ILE CYS LEU LYS VAL ASN LYS VAL ILE ILE
SEQRES   9 A  216  CYS GLY HIS THR ASP CYS GLY GLY ILE LYS THR CYS LEU
SEQRES  10 A  216  THR ASN GLN ARG GLU ALA LEU PRO LYS VAL ASN CYS SER
SEQRES  11 A  216  HIS LEU TYR LYS TYR LEU ASP ASP ILE ASP THR MET TYR
SEQRES  12 A  216  HIS GLU GLU SER GLN ASN LEU ILE HIS LEU LYS THR GLN
SEQRES  13 A  216  ARG GLU LYS SER HIS TYR LEU SER HIS CYS ASN VAL LYS
SEQRES  14 A  216  ARG GLN PHE ASN ARG ILE ILE GLU ASN PRO THR VAL GLN
SEQRES  15 A  216  THR ALA VAL GLN ASN GLY GLU LEU GLN VAL TYR GLY LEU
SEQRES  16 A  216  LEU TYR ASN VAL GLU ASP GLY LEU LEU GLN THR VAL SER
SEQRES  17 A  216  THR TYR THR LYS VAL THR PRO LYS
SEQRES   1 B  216  MET HIS HIS HIS HIS HIS HIS GLY HIS ASN SER ASN LEU
SEQRES   2 B  216  GLN ASP ILE LEU ALA ALA ASN ALA LYS TRP ALA SER GLN
SEQRES   3 B  216  MET ASN ASN ILE GLN PRO THR LEU PHE PRO ASP HIS ASN
SEQRES   4 B  216  ALA LYS GLY GLN SER PRO HIS THR LEU PHE ILE GLY CYS
SEQRES   5 B  216  SER ASP SER ARG TYR ASN GLU ASN CYS LEU GLY VAL LEU
SEQRES   6 B  216  PRO GLY GLU VAL PHE THR TRP LYS ASN VAL ALA ASN ILE
SEQRES   7 B  216  CYS HIS SER GLU ASP LEU THR LEU LYS ALA THR LEU GLU
SEQRES   8 B  216  PHE ALA ILE ILE CYS LEU LYS VAL ASN LYS VAL ILE ILE
SEQRES   9 B  216  CYS GLY HIS THR ASP CYS GLY GLY ILE LYS THR CYS LEU
SEQRES  10 B  216  THR ASN GLN ARG GLU ALA LEU PRO LYS VAL ASN CYS SER
SEQRES  11 B  216  HIS LEU TYR LYS TYR LEU ASP ASP ILE ASP THR MET TYR
SEQRES  12 B  216  HIS GLU GLU SER GLN ASN LEU ILE HIS LEU LYS THR GLN
SEQRES  13 B  216  ARG GLU LYS SER HIS TYR LEU SER HIS CYS ASN VAL LYS
SEQRES  14 B  216  ARG GLN PHE ASN ARG ILE ILE GLU ASN PRO THR VAL GLN
SEQRES  15 B  216  THR ALA VAL GLN ASN GLY GLU LEU GLN VAL TYR GLY LEU
SEQRES  16 B  216  LEU TYR ASN VAL GLU ASP GLY LEU LEU GLN THR VAL SER
SEQRES  17 B  216  THR TYR THR LYS VAL THR PRO LYS
HET     ZN  A   1       1
HET    ACT  A 222       4
HET    ACT  A   2       4
HET    EDO  A   3       4
HET    EDO  A   4       4
HET     ZN  B   2       1
HET    EDO  B   1       4
HET    EDO  B 222       4
HETNAM      ZN ZINC ION
HETNAM     ACT ACETATE ION
HETNAM     EDO 1,2-ETHANEDIOL
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   3   ZN    2(ZN 2+)
FORMUL   4  ACT    2(C2 H3 O2 1-)
FORMUL   6  EDO    4(C2 H6 O2)
FORMUL  11  HOH   *152(H2 O)
HELIX    1   1 ASN A   17  GLN A   36  1                                  20
HELIX    2   2 PRO A   37  PHE A   40  5                                   4
HELIX    3   3 ASN A   63  GLY A   68  5                                   6
HELIX    4   4 VAL A   80  ILE A   83  5                                   4
HELIX    5   5 ASP A   88  CYS A  101  1                                  14
HELIX    6   6 CYS A  115  THR A  123  1                                   9
HELIX    7   7 GLN A  125  ASN A  133  5                                   9
HELIX    8   8 CYS A  134  LEU A  141  1                                   8
HELIX    9   9 LEU A  141  GLU A  151  1                                  11
HELIX   10  10 GLU A  151  ILE A  156  1                                   6
HELIX   11  11 THR A  160  ILE A  181  1                                  22
HELIX   12  12 ASN A  183  ASN A  192  1                                  10
HELIX   13  13 ASN B   17  GLN B   36  1                                  20
HELIX   14  14 PRO B   37  PHE B   40  5                                   4
HELIX   15  15 ASN B   63  GLY B   68  5                                   6
HELIX   16  16 VAL B   80  ILE B   83  5                                   4
HELIX   17  17 ASP B   88  CYS B  101  1                                  14
HELIX   18  18 CYS B  115  THR B  123  1                                   9
HELIX   19  19 GLN B  125  ASN B  133  5                                   9
HELIX   20  20 CYS B  134  LEU B  141  1                                   8
HELIX   21  21 LEU B  141  GLU B  151  1                                  11
HELIX   22  22 THR B  160  ILE B  181  1                                  22
HELIX   23  23 ASN B  183  ASN B  192  1                                  10
SHEET    1   A 5 VAL A  74  ASN A  79  0
SHEET    2   A 5 THR A  52  CYS A  57  1  N  PHE A  54   O  PHE A  75
SHEET    3   A 5 LYS A 106  HIS A 112  1  O  CYS A 110   N  ILE A  55
SHEET    4   A 5 GLN A 196  TYR A 202  1  O  LEU A 200   N  ILE A 109
SHEET    5   A 5 LEU A 209  TYR A 215 -1  O  SER A 213   N  GLY A 199
SHEET    1   B 5 VAL B  74  ASN B  79  0
SHEET    2   B 5 THR B  52  CYS B  57  1  N  PHE B  54   O  PHE B  75
SHEET    3   B 5 LYS B 106  HIS B 112  1  O  CYS B 110   N  ILE B  55
SHEET    4   B 5 GLN B 196  TYR B 202  1  O  LEU B 200   N  ILE B 109
SHEET    5   B 5 LEU B 209  TYR B 215 -1  O  SER B 213   N  GLY B 199
LINK         SG  CYS A  57                ZN    ZN A   1     1555   1555  2.34
LINK         NE2 HIS A 112                ZN    ZN A   1     1555   1555  2.03
LINK         SG  CYS A 115                ZN    ZN A   1     1555   1555  2.24
LINK         SG  CYS B  57                ZN    ZN B   2     1555   1555  2.23
LINK         NE2 HIS B 112                ZN    ZN B   2     1555   1555  2.06
LINK         SG  CYS B 115                ZN    ZN B   2     1555   1555  2.40
LINK        ZN    ZN A   1                 O   HOH A 263     1555   1555  2.18
LINK        ZN    ZN B   2                 O   HOH A 300     1555   1555  2.02
SITE     1 AC1  5 CYS A  57  HIS A 112  CYS A 115  ACT A 222
SITE     2 AC1  5 HOH A 263
SITE     1 AC2 11  ZN A   1  CYS A  57  VAL A  80  ALA A  81
SITE     2 AC2 11 CYS A 115  GLY A 116  GLY A 117  HOH A 257
SITE     3 AC2 11 HOH A 263  PHE B  75  PHE B  97
SITE     1 AC3 11 PHE A  75  PHE A  97  HOH A 299  HOH A 300
SITE     2 AC3 11  ZN B   2  CYS B  57  VAL B  80  ALA B  81
SITE     3 AC3 11 CYS B 115  GLY B 116  GLY B 117
SITE     1 AC4  4 HIS A  85  SER A  86  ARG A 179  HOH A 289
SITE     1 AC5  5 PRO A 184  THR A 188  HOH A 275  HOH A 277
SITE     2 AC5  5 GLU B  87
SITE     1 AC6  5 ACT A   2  HOH A 300  CYS B  57  HIS B 112
SITE     2 AC6  5 CYS B 115
SITE     1 AC7  5 HIS B  85  SER B  86  ARG B 179  HOH B 264
SITE     2 AC7  5 HOH B 292
SITE     1 AC8  6 THR B 113  HIS B 166  ASN B 203  GLU B 205
SITE     2 AC8  6 HOH B 269  HOH B 293
CRYST1   60.570  155.730   89.690  90.00  90.00  90.00 C 2 2 21     16
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.016510  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006421  0.000000        0.00000
SCALE3      0.000000  0.000000  0.011150        0.00000
      
PROCHECK
Go to PROCHECK summary
 References